Reviewed, UniProtKB/Swiss-Prot P24472 (GSTA4_MOUSE)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase A4
    EC=2.5.1.18
Alternative name(s):
    GST A4-4
      Short name=GSTA4-4
    Glutathione S-transferase 5.7
      Short name=GST 5.7
    GST class-alpha member 4

Gene names

Name:	Gsta4
Synonyms:	Gsta

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Post-translational modification	The N-terminus is blocked.
Miscellaneous	On the basis of immunological and kinetics data, GST 5.7 is distinct from alpha, mu and pI classes of GTS. However it has been postulated that this protein may be part of a distinct subgroup within this alpha class. The variations were found from AA sequencing and imply there are multiple forms of this protein. These variations are likely to be sex-linked and tissue specific.
Sequence similarities	Belongs to the GST superfamily. Alpha family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutathione transferase activity Ref.1 Traceable author statement. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 222

222

Glutathione S-transferase A4

PRO_0000185791

Regions

Domain

3 – 83

81

GST N-terminal

Domain

85 – 208

124

GST C-terminal

Natural variations

Natural variant

115

1

K → P Requires 2 nucleotide substitutions.

Natural variant

167

1

V → G

Natural variant

179 – 180

2

PL → GE

Experimental info

Sequence conflict

36

1

E → D in BAB31640. Ref.2

Sequence conflict

205 – 206

2

KP → SA in BAB27873. Ref.2

Sequence conflict

218

1

T → I in AAA37754. Ref.1

Secondary structure

1

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222

Helix Strand Turn

Details...

Beta strand

6 – 9

4

Turn

14 – 16

3

Helix

17 – 26

10

Helix

38 – 45

8

Turn

46 – 48

3

Beta strand

50 – 53

4

Beta strand

57 – 60

4

Beta strand

63 – 65

3

Helix

68 – 78

11

Helix

86 – 108

23

Helix

109 – 111

3

Helix

114 – 131

18

Helix

133 – 142

10

Beta strand

145 – 152

8

Helix

155 – 168

14

Helix

174 – 177

4

Helix

179 – 189

11

Helix

192 – 198

7

Helix

210 – 219

10

Sequences

	Sequence		Length	Mass (Da)
	P24472-1 [UniParc]. Last modified January 23, 2002. Version 3. Checksum: B580E3415289424D	FASTA	222	25,564
	10 20 30 40 50 60 MAAKPKLYYF NGRGRMESIR WLLAAAGVEF EEEFLETREQ YEKMQKDGHL LFGQVPLVEI 70 80 90 100 110 120 DGMMLTQTRA ILSYLAAKYN LYGKDLKERV RIDMYADGTQ DLMMMIAVAP FKTPKEKEES 130 140 150 160 170 180 YDLILSRAKT RYFPVFEKIL KDHGEAFLVG NQLSWADIQL LEAILMVEEL SAPVLSDFPL 190 200 210 220 LQAFKTRISN IPTIKKFLQP GSQRKPPPDG PYVEVVRTVL KF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A subgroup of class alpha glutathione S-transferases. Cloning of cDNA for mouse lung glutathione S-transferase GST 5.7." Zimniak P., Eckles M.A., Saxena M., Awasthi Y.C. FEBS Lett. 313:173-176(1992) [PubMed: 1426286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo, Small intestine and Tongue.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Characterization of a novel glutathione S-transferase isoenzyme from mouse lung and liver having structural similarity to rat glutathione S-transferase 8-8." Medh R.D., Saxena M., Singhal S.S., Ahmad H., Awasthi Y.C. Biochem. J. 278:793-799(1991) [PubMed: 1898365] [Abstract] Cited for: PROTEIN SEQUENCE OF 106-120 AND 167-184. Strain: CD-1. Tissue: Liver and Lung.
[5]	"Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress." Krengel U., Schroter K.H., Hoier H., Arkema A., Kalk K.H., Zimniak P., Dijkstra B.W. FEBS Lett. 422:285-290(1998) [PubMed: 9498801] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). Tissue: Lung.
[6]	"Crystal structure of a murine glutathione S-transferase in complex with a glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: evidence of signaling across the dimer interface." Xiao B., Singh S.P., Nanduri B., Awasthi Y.C., Zimniak P., Ji X. Biochemistry 38:11887-11894(1999) [PubMed: 10508391] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). Tissue: Lung.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L06047 mRNA. Translation: AAA37754.1.
AK008189 mRNA. Translation: BAB25520.1.
AK008193 mRNA. Translation: BAB25524.1.
AK008400 mRNA. Translation: BAB25649.1.
AK008490 mRNA. Translation: BAB25696.1.
AK009668 mRNA. Translation: BAB26429.1.
AK010098 mRNA. Translation: BAB26701.1.
AK011177 mRNA. Translation: BAB27449.1.
AK011841 mRNA. Translation: BAB27873.1.
AK019100 mRNA. Translation: BAB31546.1.
AK019271 mRNA. Translation: BAB31640.1.
BC012639 mRNA. Translation: AAH12639.1.

IPI

IPI00323911.

PIR

S27234.

RefSeq

NP_034487.2.

UniGene

Mm.2662

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B48	X-ray	2.60	A/B	2-222	[»]
1GUK	X-ray	2.90	A/B	1-222	[»]

ModBase

Search...

PTM databases

PhosphoSite

P24472.

2-D gel databases

REPRODUCTION-2DPAGE

P24472.

Proteomic databases

PRIDE

P24472.

Genome annotation databases

Ensembl

ENSMUSG00000032348. Mus musculus. [Contig view]

GeneID

14860.

KEGG

mmu:14860.

NMPDR

fig|10090.3.peg.20538.

Organism-specific databases

MGI

MGI:1309515. Gsta4.

Phylogenomic databases

HOGENOM

P24472.

HOVERGEN

P24472.

OMA

P24472. DMYADGT.

Enzyme and pathway databases

BRENDA

2.5.1.18. 244.

Gene expression databases

ArrayExpress

P24472.

Bgee

P24472.

CleanEx

MM_GSTA4.

GermOnline

ENSMUSG00000032348. Mus musculus.

Family and domain databases

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

PANTHER

PTHR11571:SF4. GST_alpha. 1 hit.

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PRINTS

PR01266. GSTRNSFRASEA.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00143. Glutathione.

NextBio

287101.

SOURCE

Search...

Entry information

Entry name

GSTA4_MOUSE

Accession

Primary (citable) accession number: P24472
Secondary accession number(s): Q9CQ81 , Q9CTY7, Q9CY87, Q9D038

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 23, 2002
Last modified:	June 16, 2009
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)